Lead, cadmium, zinc and mercury-transporting ATPase

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P37617 (ATZN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Lead, cadmium, zinc and mercury-transporting ATPase
EC=3.6.3.3
EC=3.6.3.5

Gene names

Name:	zntA
Synonyms:	yhhO
Ordered Locus Names:	b3469, JW3434

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in export of lead, cadmium, zinc and mercury.
Catalytic activity	ATP + H₂O + Cd²⁺(In) = ADP + phosphate + Cd²⁺(Out). ATP + H₂O + Zn²⁺(In) = ADP + phosphate + Zn²⁺(Out).
Subcellular location	Cell inner membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification] Contains 1 HMA domain.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Cadmium Magnesium Mercury Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	detoxification of zinc ion Inferred from mutant phenotype Ref.4. Source: EcoliWiki response to cadmium ion Inferred from mutant phenotype Ref.4. Source: EcoliWiki
Cellular_component	integral to membrane Inferred from direct assay Ref.4. Source: EcoCyc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cadmium-exporting ATPase activity Inferred from direct assay Ref.6. Source: EcoCyc cobalt ion transmembrane transporter activity Inferred from mutant phenotype Ref.5. Source: EcoCyc lead ion transmembrane transporter activity Inferred from mutant phenotype Ref.5. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel cation transmembrane transporter activity Inferred from mutant phenotype Ref.5. Source: EcoCyc zinc-exporting ATPase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 732

732

Lead, cadmium, zinc and mercury-transporting ATPase

PRO_0000046332

Regions

Topological domain

1 – 124

124

Periplasmic Potential

Transmembrane

125 – 145

Helical; Potential

Topological domain

146 – 191

Cytoplasmic Potential

Transmembrane

192 – 212

Helical; Potential

Topological domain

213 – 356

144

Periplasmic Potential

Transmembrane

357 – 377

Helical; Potential

Topological domain

378 – 383

Cytoplasmic Potential

Transmembrane

384 – 404

Helical; Potential

Topological domain

405 – 461

Periplasmic Potential

Transmembrane

462 – 482

Helical; Potential

Topological domain

483 – 632

150

Cytoplasmic Potential

Transmembrane

633 – 653

Helical; Potential

Topological domain

654 – 693

Periplasmic Potential

Transmembrane

694 – 714

Helical; Potential

Topological domain

715 – 732

Cytoplasmic Potential

Domain

49 – 113

HMA

Sites

Active site

436

4-aspartylphosphate intermediate By similarity

Metal binding

Zinc

Metal binding

Zinc

Metal binding

Zinc

Metal binding

628

Magnesium By similarity

Metal binding

632

Magnesium By similarity

Secondary structure

732

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37617 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 25476EA830786465
Show »

FASTA

732

76,840

        10         20         30         40         50         60 
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY SWKVSGMDCA 

        70         80         90        100        110        120 
ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV ESALQKAGYS LRDEQAAEEP 

       130        140        150        160        170        180 
QASRLKENLP LITLIVMMAI SWGLEQFNHP FGQLAFIATT LVGLYPIARQ ALRLIKSGSY 

       190        200        210        220        230        240 
FAIETLMSVA AIGALFIGAT AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT 

       250        260        270        280        290        300 
RLRKGEREEV AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD 

       310        320        330        340        350        360 
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF SRIYTPAIMA 

       370        380        390        400        410        420 
VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST PAAITSGLAA AARRGALIKG 

       430        440        450        460        470        480 
GAALEQLGRV TQVAFDKTGT LTVGKPRVTA IHPATGISES ELLTLAAAVE QGATHPLAQA 

       490        500        510        520        530        540 
IVREAQVAEL AIPTAESQRA LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ 

       550        560        570        580        590        600 
TVVLVVRNDD VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE 

       610        620        630        640        650        660 
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD VALETADAAL 

       670        680        690        700        710        720 
THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT LLGMTGLWLA VLADTGATVL 

       730 
VTANALRLLR RR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase." Rensing C., Mitra B., Rosen B.P. Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase." Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K. Mol. Microbiol. 25:883-891(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli." Sharma R., Rensing C., Rosen B.P., Mitra B. J. Biol. Chem. 275:3873-3878(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[8]	"A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)." Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V. J. Mol. Biol. 323:883-897(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.

PIR

S47688.

RefSeq

NP_417926.1. NC_000913.2.
YP_491965.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MWY	NMR	-	A	46-118	[»]
1MWZ	NMR	-	A	46-118	[»]

ProteinModelPortal

P37617.

SMR

P37617. Positions 46-118, 213-728.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-12947N.

IntAct

P37617. 8 interactions.

MINT

MINT-1256950.

STRING

511145.b3469.

Protein family/group databases

TCDB

3.A.3.6.2. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PaxDb

P37617.

PRIDE

P37617.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.

GeneID

12933927.
947972.

KEGG

ecj:Y75_p3709.
eco:b3469.

PATRIC

32122382. VBIEscCol129921_3568.

Organism-specific databases

EchoBASE

EB2129.

EcoGene

EG12215. zntA.

Phylogenomic databases

eggNOG

COG2217.

HOGENOM

HOG000250399.

K01534.

OMA

AWLPWIY.

ProtClustDB

PRK11033.

Enzyme and pathway databases

BioCyc

EcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.

Gene expression databases

Genevestigator

P37617.

Family and domain databases

Gene3D

2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.

InterPro

IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR027265. Di_cation_transp_P_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]

PANTHER

PTHR24093. PTHR24093. 1 hit.
PTHR24093:SF126. PTHR24093:SF126. 1 hit.

Pfam

PF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.
PR00120. HATPASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.

TIGRFAMs

TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P37617.

Entry information

Entry name

ATZN_ECOLI

Accession

Primary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents